Research workbench
AlphaFold monomer V2.0 prediction for protein-arginine N-acetylglucosaminyltransferase nleb (A0A482PDI9)
Analyse AlphaFold monomer V2.0 prediction for protein-arginine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A482PDI9
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3Abe1980007F3787fAfC5f8C1F4951B45508443D
- Molecule
- Protein-arginine N-acetylglucosaminyltransferase nleb
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-arginine N-acetylglucosaminyltransferase nleb | protein | 329 | 37% helix, 20% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.67 | 0.83 | 33 | empty |
| 2 | 211 | 0.51 | 0.76 | 20 | empty |
| 3 | 76 | 0.35 | 0.76 | 18 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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